Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome

UCSF Chimera—A visualization system for exploratory research and analysis

Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,047

Coot : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571

PHENIX : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716

Inference of Macromolecular Assemblies from Crystalline State

Krissinel, E., & Henrick, K. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.05.022 · Cited by 10,007

MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Zheng, S. Q., Palovcak, E. J., Armache, J., Verba, K. A., Cheng, Y., & Agard, D. A. (2017) · Nature Methods · doi:10.1038/nmeth.4193 · Cited by 7,496

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkòczi, G., Chen, V. B., Davis, I., Echols, N., Headd, J. J., Hung, L., Kapral, G. J., Grosse‐Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334

Automated electron microscope tomography using robust prediction of specimen movements

Mastronarde, D. N. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,136

The ubiquitin code

Komander, D., & Rape, M. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060310-170328 · Cited by 3,679

Gctf: Real-time CTF determination and correction

Zhang, K. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.11.003 · Cited by 3,417

Structure of 20S proteasome from yeast at 2.4Å resolution

Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D., & Huber, R. (1997) · Nature · doi:10.1038/386463a0 · Cited by 2,265

An expanded lexicon for the ubiquitin code

Đikić, I., & Schulman, B. A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00543-1 · Cited by 426

Antigen presentation in cancer — mechanisms and clinical implications for immunotherapy

Yang, K., Halima, A., & Chan, T. A.-T. (2023) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-023-00789-4 · Cited by 352

Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding

Twomey, E. C., Ji, Z., Wales, T. E., Bodnar, N. O., Ficarro, S. B., Marto, J. A., Engen, J. R., & Rapoport, T. A. (2019) · Science · doi:10.1126/science.aax1033 · Cited by 293

Functional Modules of the Proteostasis NetworkPreprint

Jayaraj, G. G., Hipp, M. S., & Hartl, F. U. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033951 · Cited by 254

The molecular principles governing the activity and functional diversity of AAA+ proteins

Puchades, C., Sandate, C. R., & Lander, G. C. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0183-6 · Cited by 239

Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation

Marshall, R. S., & Vierstra, R. D. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00040 · Cited by 243

DeepTracer for fast de novo cryo-EM protein structure modeling and special studies on CoV-related complexes

Pfab, J., Phan, N. M., & Si, D. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017525118 · Cited by 198

Deep learning-based mixed-dimensional Gaussian mixture model for characterizing variability in cryo-EM

Chen, M., & Ludtke, S. J. (2021) · Nature Methods · doi:10.1038/s41592-021-01220-5 · Cited by 186

Developments, applications, and prospects of cryo‐electron microscopy

Xu, B., & Ling, L. (2019) · Protein Science · doi:10.1002/pro.3805 · Cited by 170

Structure of the Cdc48 segregase in the act of unfolding an authentic substrate

Cooney, I., Han, H., Stewart, M. G., Carson, R. H., Hansen, D. T., Iwasa, J., Price, J. C., Hill, C. P., & Shen, P. S. (2019) · Science · doi:10.1126/science.aax0486 · Cited by 166

Structures of the ATP-fueled ClpXP proteolytic machine bound to protein substrate

Fei, X., Bell, T. A., Jenni, S., Stinson, B. M., Baker, T. A., Harrison, S. C., & Sauer, R. T. (2020) · eLife · doi:10.7554/elife.52774 · Cited by 144

The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag

Sahu, I., Mali, S. M., Sulkshane, P., Xu, C., Rozenberg, A., Morag, R., Sahoo, M. P., Singh, S. K., Ding, Z., Wang, Y., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26427-0 · Cited by 146

The 26S Proteasome Utilizes a Kinetic Gateway to Prioritize Substrate Degradation

Bard, J. A. M., Bashore, C., Dong, K. C., & Martin, A. (2019) · Cell · doi:10.1016/j.cell.2019.02.031 · Cited by 137

The AAA+ superfamily: a review of the structural and mechanistic principles of these molecular machines

Khan, Y. A., White, K. I., & Brünger, A. T. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1979460 · Cited by 128

Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP‐dependent substrate translocation

Gates, S. N., & Martin, A. (2019) · Protein Science · doi:10.1002/pro.3743 · Cited by 127

Processive extrusion of polypeptide loops by a Hsp100 disaggregase

Avellaneda, M. J., Franke, K. B., Šunderlíková, V., Bukau, B., Mogk, A., & Tans, S. J. (2020) · Nature · doi:10.1038/s41586-020-1964-y · Cited by 130

AKIRIN2 controls the nuclear import of proteasomes in vertebrates

de Almeida, M., Hinterndorfer, M., Brunner, H. L., Grishkovskaya, I., Singh, K., Schleiffer, A., Jude, J., Deswal, S., Kalis, R., Vunjak, M., et al. (2021) · Nature · doi:10.1038/s41586-021-04035-8 · Cited by 123

Targeted degradation via direct 26S proteasome recruitment

Bashore, C., Prakash, S., Johnson, M. C., Conrad, R. J., Kekessie, I. A., Scales, S. J., Ishisoko, N., Kleinheinz, T., Liu, P. S., Popovych, N., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01218-w · Cited by 126

The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges

Tundo, G. R., Sbardella, D., Santoro, A. M., Coletta, A., Oddone, F., Grasso, G., Milardi, D., Lacal, P. M., Marini, S., Purrello, R., et al. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107579 · Cited by 120

USP14-regulated allostery of the human proteasome by time-resolved cryo-EM

Zhang, S., Zou, S., Yin, D., Zhao, L., Finley, D. J., Wu, Z., & Mao, Y. (2022) · Nature · doi:10.1038/s41586-022-04671-8 · Cited by 112

Deep Learning to Predict Protein Backbone Structure from High-Resolution Cryo-EM Density Maps

Si, D., Moritz, S. A., Pfab, J., Hou, J., Cao, R., Wang, L., Wu, T., & Cheng, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-60598-y · Cited by 106

Targeted protein degradation directly engaging lysosomes or proteasomes

Kim, J., Byun, I., Kim, D. Y., Joh, H., Kim, H. J., & Lee, M. J. (2024) · Chemical Society Reviews · doi:10.1039/d3cs00344b · Cited by 108

The pre-synaptic fusion machinery

Brünger, A. T., Choi, U. B., Lai, Y., Leitz, J., White, K. I., & Zhou, Q. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.03.007 · Cited by 107

Mechanisms and regulation of substrate degradation by the 26S proteasome

Arkinson, C., Dong, K. C., Gee, C. L., & Martin, A. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00778-0 · Cited by 115

Structure, Dynamics and Function of the 26S Proteasome

Mao, Y. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_1 · Cited by 111

Proteasome in action: substrate degradation by the 26S proteasome

Sahu, I., & Glickman, M. H. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200382 · Cited by 101

Molecular Basis for ATP-Hydrolysis-Driven DNA Translocation by the CMG Helicase of the Eukaryotic Replisome

Eickhoff, P., Kose, H. B., Martino, F., Petojevic, T., Ali, F. A., Locke, J., Tamberg, N., Nans, A., Berger, J., Botchan, M., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.104 · Cited by 84

Ubiquitin–proteasome system and the role of its inhibitors in cancer therapy

Aliabadi, F., Sohrabi, B., Mostafavi, E., Pazoki–Toroudi, H., & Webster, T. J. (2021) · Open Biology · doi:10.1098/rsob.200390 · Cited by 101

Proteasome Inhibition Activates Autophagy-Lysosome Pathway Associated With TFEB Dephosphorylation and Nuclear Translocation

Li, C., Wang, X., Li, X., Qiu, K., Jiao, F., Liu, Y., Kong, Q., Liu, Y., & Wu, Y. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00170 · Cited by 93

The proteasome and its role in the nervous system

Türker, F., Cook, E. K., & Margolis, S. S. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.04.003 · Cited by 101

Integration of Mass Spectrometry Data for Structural Biology

Britt, H. M., Cragnolini, T., & Thalassinos, K. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00356 · Cited by 87

Mechanisms of σ54-Dependent Transcription Initiation and Regulation

Danson, A. E., Jovanovic, M., Buck, M., & Zhang, X. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.04.022 · Cited by 84

The Proteasome and Its Network: Engineering for AdaptabilityPreprint

Finley, D. J., & Prado, M. A. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033985 · Cited by 86

K29-linked ubiquitin signaling regulates proteotoxic stress response and cell cycle

Yu, Y., Zheng, Q., Erramilli, S. K., Pan, M., Park, S.-J., Xie, Y., Li, J., Fei, J., Kossiakoff, A. A., Liu, L., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00823-5 · Cited by 82

Nanoarchitectonics from Atom to Life

Ariga, K., & Yamauchi, Y. (2020) · Chemistry - An Asian Journal · doi:10.1002/asia.202000106 · Cited by 80

Structural basis for distinct operational modes and protease activation in AAA+ protease Lon

Shin, M., Puchades, C., Asmita, A., Puri, N., Adjei, E., Wiseman, R. L., Karzai, A. W., & Lander, G. C. (2020) · Science Advances · doi:10.1126/sciadv.aba8404 · Cited by 76

Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation

Collins, G. A., & Goldberg, A. L. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1915534117 · Cited by 76

A modular toolbox to generate complex polymeric ubiquitin architectures using orthogonal sortase enzymes

Fottner, M., Weyh, M., Gaussmann, S., Schwarz, D., Sattler, M., & Lang, K. (2021) · Nature Communications · doi:10.1038/s41467-021-26812-9 · Cited by 73

Ubiquitin Signaling and Degradation of Aggregate-Prone Proteins

Galves, M., Rathi, R., Prag, G., & Ashkenazi, A. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.04.007 · Cited by 73

Proteotoxic Stress and Cell Death in Cancer Cells

Brancolini, C., & Iuliano, L. (2020) · Cancers · doi:10.3390/cancers12092385 · Cited by 73

Membranes under the Magnetic Lens: A Dive into the Diverse World of Membrane Protein Structures Using Cryo-EM

Piper, S. J., Johnson, R. M., Wootten, D. L., & Sexton, P. M. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00837 · Cited by 78

Structural Snapshots of 26S Proteasome Reveal Tetraubiquitin-Induced Conformations

Ding, Z., Xu, C., Sahu, I., Wang, Y., Fu, Z., Huang, M., Wong, C. C. L., Glickman, M. H., & Cong, Y. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.018 · Cited by 69

Structural Insights into Substrate Recognition and Processing by the 20S Proteasome

Sahu, I., & Glickman, M. H. (2021) · Biomolecules · doi:10.3390/biom11020148 · Cited by 69

Mechanisms of substrate recognition by the 26S proteasome

Davis, C., Spaller, B. L., & Matouschek, A. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.010 · Cited by 66

Dual Functions of a Rubisco Activase in Metabolic Repair and Recruitment to Carboxysomes

Flecken, M., Wang, H., Popilka, L., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. K. (2020) · Cell · doi:10.1016/j.cell.2020.09.010 · Cited by 66

Comparative Structural Analysis of 20S Proteasome Ortholog Protein Complexes by Native Mass Spectrometry

Vimer, S., Ben-Nissan, G., Morgenstern, D., Kumar-Deshmukh, F., Polkinghorn, C., Quintyn, R. S., Vasil’ev, Y. V., Beckman, J. S., Elad, N., Wysocki, V. H., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00080 · Cited by 63

Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis

Lopez, K. E., Rizo, A. N., Tse, E., Lin, J., Scull, N. W., Thwin, A. C., Lucius, A. L., Shorter, J., & Southworth, D. R. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0409-5 · Cited by 63

Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor

Deville, C., Franke, K. B., Mogk, A., Bukau, B., & Saibil, H. R. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.075 · Cited by 63

AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms

Zhang, S., & Mao, Y. (2020) · Biomolecules · doi:10.3390/biom10040629 · Cited by 64

Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction

Wang, L., Myasnikov, A. G., Pan, X., & Walter, P. (2020) · eLife · doi:10.7554/elife.54031 · Cited by 55

Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies

Chen, X., Htet, Z. M., López-Alfonzo, E. M., Martin, A., & Walters, K. J. (2020) · FEBS Journal · doi:10.1111/febs.15638 · Cited by 61

Protein degradation: expanding the toolbox to restrain cancer drug resistance

Ming, H., Li, B., Jiang, J., Qin, S., Nice, E. C., He, W., Lang, T., & Huang, C. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-023-01398-5 · Cited by 64

Inhibition of dual-specificity tyrosine phosphorylation-regulated kinase 2 perturbs 26S proteasome-addicted neoplastic progression

Banerjee, S., Wei, T., Wang, J., Lee, J. J., Gutierrez, H. L., Chapman, O. S., Wiley, S. E., Mayfield, J. E., Tandon, V., Juarez, E. F., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912033116 · Cited by 60

PA28γ: New Insights on an Ancient Proteasome Activator

Cascio, P. (2021) · Biomolecules · doi:10.3390/biom11020228 · Cited by 59

Molecular and cellular dynamics of the 26S proteasome

Sakata, E., Eisele, M. R., & Baumeister, W. P. (2020) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2020.140583 · Cited by 57

Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10

Buel, G. R., Chen, X., Chari, R., O’Neill, M. J., Ebelle, D. L., Jenkins, C., Sridharan, V., Tarasov, S. G., Tarasova, N. I., Andrésson, Þ., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15073-7 · Cited by 55

Efficiency of the four proteasome subtypes to degrade ubiquitinated or oxidized proteins

Habib, J. A., Plaen, E. D., Stroobant, V., Živković, D., Bousquet, M., Guillaume, B., Wahni, K., Messens, J., Busse, A., Vigneron, N., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71550-5 · Cited by 55

AAA+ ATPases: structural insertions under the magnifying glass

Jessop, M., Félix, J., & Gutsche, I. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.027 · Cited by 55

Proteasome substrate receptors and their therapeutic potential

Amponsa, V. O., & Walters, K. J. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.06.006 · Cited by 55

Advances that facilitate the study of large RNA structure and dynamics by nuclear magnetic resonance spectroscopy

Zhang, H., & Keane, S. C. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1541 · Cited by 54

Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function

Liu, X., Xiao, W., Zhang, Y., Wiley, S. E., Zuo, T., Zheng, Y., Chen, N., Chen, L., Wang, X., Zheng, Y., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912531117 · Cited by 55

A large expert-curated cryo-EM image dataset for machine learning protein particle picking

Dhakal, A., Gyawali, R., Wang, L., & Cheng, J. J. (2023) · Scientific Data · doi:10.1038/s41597-023-02280-2 · Cited by 54

Simulation-Based Methods for Model Building and Refinement in Cryoelectron Microscopy

Dodd, T., Yan, C., & Ivanov, I. N. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00087 · Cited by 52

Nanoarchitectonics beyond perfect order – not quite perfect but quite useful

Cao, L., Huang, Y., Parakhonskiy, B. V., & Skirtach, A. G. (2022) · Nanoscale · doi:10.1039/d2nr02537j · Cited by 48

Understanding the 26S proteasome molecular machine from a structural and conformational dynamics perspective

Greene, E. R., Dong, K. C., & Martin, A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.004 · Cited by 51

Immunoproteasome-selective inhibitors: An overview of recent developments as potential drugs for hematologic malignancies and autoimmune diseases

Xi, J., Zhuang, R., Kong, L., He, R., Zhu, H., & Zhang, J. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111646 · Cited by 48

Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein

Tang, W. K., Borgnia, M. J., Hsu, A. L., Esser, L., Fox, T. L., de Val, N., & Xia, D. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0373-0 · Cited by 48

Deubiquitination Reactions on the Proteasome for Proteasome Versatility

Shin, J. Y., Muniyappan, S., Tran, N.-N., Park, H., Lee, S. B., & Lee, B. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21155312 · Cited by 50

Degradation of SERRATE via ubiquitin-independent 20S proteasome to survey RNA metabolism

Li, Y., Sun, D., Ma, Z., Yamaguchi, K., Wang, L., Zhong, S., Yan, X., Shang, B., Nagashima, Y., Koiwa, H., et al. (2020) · Nature Plants · doi:10.1038/s41477-020-0721-4 · Cited by 47

Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis

Sauer, R. T., Fei, X., Bell, T. A., & Baker, T. A. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1979461 · Cited by 46

Proteasomes: unfoldase-assisted protein degradation machines

Majumder, P., & Baumeister, W. P. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0344 · Cited by 48

Msp1/ATAD1 in Protein Quality Control and Regulation of Synaptic Activities

Wang, L., & Walter, P. (2020) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-031220-015840 · Cited by 48

Allosteric control of Ubp6 and the proteasome via a bidirectional switch

Hung, K. Y. S., Klumpe, S., Eisele, M. R., Elsasser, S., Tian, G., Sun, S., Moroco, J. A., Cheng, T. C., Joshi, T., Seibel, T., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28186-y · Cited by 44

Structural insights into the human PA28–20S proteasome enabled by efficient tagging and purification of endogenous proteins

Zhao, J., Makhija, S., Zhou, C., Zhang, H., Wang, Y., Muralidharan, M., Huang, B., & Cheng, Y. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207200119 · Cited by 43

Melatonin: Regulation of Biomolecular Condensates in Neurodegenerative Disorders

Loh, D., & Reiter, R. J. (2021) · Antioxidants · doi:10.3390/antiox10091483 · Cited by 45

Cryo-EM structures of Helicobacter pylori vacuolating cytotoxin A oligomeric assemblies at near-atomic resolution

Zhang, K., Zhang, H., Li, S., Pintilie, G. D., Mou, T., Gao, Y., Zhang, Q., Bedem, H. V. D., Schmid, M. F., Au, S. W. N., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821959116 · Cited by 42

Structure of spastin bound to a glutamate-rich peptide implies a hand-over-hand mechanism of substrate translocation

Han, H., Schubert, H., McCullough, J., Monroe, N., Purdy, M. D., Yeager, M. J., Sundquist, W. I., & Hill, C. P. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ac119.009890 · Cited by 42

More than an on-and-off switch: Post-translational modifications of plant pattern recognition receptor complexes

Kong, L., Rodrigues, B., Kim, J. H., He, P., & Shan, L. (2021) · Current Opinion in Plant Biology · doi:10.1016/j.pbi.2021.102051 · Cited by 41

Advances in Proteasome Enhancement by Small Molecules

George, D. E., & Tepe, J. J. (2021) · Biomolecules · doi:10.3390/biom11121789 · Cited by 42

The Conceivable Functions of Protein Ubiquitination and Deubiquitination in Reproduction

Wang, J., Zhou, Q., Ding, J., Yin, T., Ye, P., & Zhang, Y. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.886261 · Cited by 39

Structure of Vps4 with circular peptides and implications for translocation of two polypeptide chains by AAA+ ATPases

Han, H., Fulcher, J. M., Dandey, V. P., Iwasa, J., Sundquist, W. I., Kay, M. S., Shen, P. S., & Hill, C. P. (2019) · eLife · doi:10.7554/elife.44071 · Cited by 40

Proteasome Activation to Combat Proteotoxicity

Jones, C. L., & Tepe, J. J. (2019) · Molecules · doi:10.3390/molecules24152841 · Cited by 43

Two-Step Activation Mechanism of the ClpB Disaggregase for Sequential Substrate Threading by the Main ATPase Motor.

Deville, C., & Saibil, H. R. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6qs4/pdb · Cited by 38

Characterizing ATP processing by the AAA+ protein p97 at the atomic level

Shein, M., Hitzenberger, M., Cheng, T. C., Rout, S. R., Leitl, K. D., Sato, Y., Zacharias, M., Sakata, E., & Schütz, A. K. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01440-0 · Cited by 34

Substrate selection by the proteasome through initiation regions

Tomita, T., & Matouschek, A. T. (2019) · Protein Science · doi:10.1002/pro.3642 · Cited by 39

PSMC2 promotes the progression of gastric cancer via induction of RPS15A/mTOR pathway

Liu, T., Zhang, J., Chen, H., Bianba, T., Pan, Y., Wang, X., Jiang, Y. H., & Yang, Z. (2022) · Oncogenesis · doi:10.1038/s41389-022-00386-7 · Cited by 37

PSMC3 proteasome subunit variants are associated with neurodevelopmental delay and type I interferon production

Ebstein, F., Küry, S., Most, V., Rosenfelt, C., Scott-Boyer, M.-P., van Woerden, G. M., Besnard, T., Papendorf, J. J., Studencka-Turski, M., Wang, T., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abo3189 · Cited by 36

Roles of Ubiquitination and SUMOylation in DNA Damage Response

Su, S., Zhang, Y., & Liu, P. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.059 · Cited by 37

Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13 species upregulated in multiple myeloma

Lu, X., Sabbasani, V. R., Amponsa, V. O., Evans, C. N., King, J. C., Tarasov, S. G., Dyba, M., Das, S., Chan, K. C., Schwieters, C. D., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27570-4 · Cited by 35

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation

Greene, E. R., Goodall, E. A., de la Peña, A. H., Matyskiela, M. E., Lander, G. C., & Martin, A. (2019) · eLife · doi:10.7554/elife.49806 · Cited by 35

Active conformation of the p97-p47 unfoldase complex

Xu, Y. J., Han, H., Cooney, I., Guo, Y., Moran, N. G., Zuniga, N. R., Price, J. C., Hill, C. P., & Shen, P. S. (2022) · Nature Communications · doi:10.1038/s41467-022-30318-3 · Cited by 35

Protein quality control by the proteasome and autophagy: A regulatory role of ubiquitin and liquid-liquid phase separation

Lei, L., Wu, Z., & Winklhofer, K. F. (2020) · Matrix Biology · doi:10.1016/j.matbio.2020.11.003 · Cited by 33

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Thomas, T. A., Salcedo-Tacuma, D., & Smith, D. M. (2023) · Biomolecules · doi:10.3390/biom13091326 · Cited by 33

Visualizing chaperone-mediated multistep assembly of the human 20S proteasome

Adolf, F., Du, J., Goodall, E. A., Walsh, R. M., Rawson, S., von Gronau, S., Harper, J. W., Hanna, J., & Schulman, B. A. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01268-9 · Cited by 33

An Extended Conformation for K48 Ubiquitin Chains Revealed by the hRpn2:Rpn13:K48-Diubiquitin Structure

Lu, X., Ebelle, D. L., Matsuo, H., & Walters, K. J. (2020) · Structure · doi:10.1016/j.str.2020.02.007 · Cited by 33

Mechanism of AAA+ ATPase-mediated RuvAB–Holliday junction branch migration

Wald, J., Fahrenkamp, D., Goessweiner‐Mohr, N., Lugmayr, W., Ciccarelli, L., Vesper, O., & Marlovits, T. C. (2022) · Nature · doi:10.1038/s41586-022-05121-1 · Cited by 31

Three-dimensional reconstruction of individual helical nano-filament structures from atomic force microscopy topographs

Lutter, L., Serpell, C. J., Tuite, M. F., Serpell, L. C., & Xue, W. (2020) · BioMolecular Concepts · doi:10.1515/bmc-2020-0009 · Cited by 31

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Fiolek, T. J., Keel, K. L., & Tepe, J. J. (2021) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00099 · Cited by 31

McsB forms a gated kinase chamber to mark aberrant bacterial proteins for degradation

Hajdusits, B., Suskiewicz, M. J., Hundt, N., Meinhart, A., Kurzbauer, R., Leodolter, J., Kukura, P., & Clausen, T. (2021) · eLife · doi:10.7554/elife.63505 · Cited by 28

Improving resolution and resolvability of single-particle cryoEM structures using Gaussian mixture models

Chen, M., Schmid, M. F., & Chiu, W. (2023) · Nature Methods · doi:10.1038/s41592-023-02082-9 · Cited by 29

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de la Peña, A. H., Goodall, E. A., Gates, S. N., Lander, G. C., & Martin, A. (2018) · Science · doi:10.1126/science.aav0725 · Cited by 296

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Mao, Y. (2020) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-58971-4_1 · Cited by 111

Molecular mechanisms of substrate degradation by the 26S proteasome revealed by CryoEM (952.6)

Matyskiela, M. E., Lander, G. C., & Martin, A. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.952.6

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Greene, E. R., Dong, K. C., & Martin, A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.10.004 · Cited by 51

Substrate degradation by the 26S proteasome (478.2)

Martin, A., Matyskiela, M. E., Beckwith, R., Nyquist, K., Worden, E. J., Estrin, E., & Lander, G. C. (2014) · The FASEB Journal · doi:10.1096/fasebj.28.1_supplement.478.2